PCYT1B

Protein-coding gene in the species Homo sapiens
PCYT1B
Identifiers
AliasesPCYT1B, CCTB, CTB, phosphate cytidylyltransferase 1, choline, beta, phosphate cytidylyltransferase 1B, choline
External IDsOMIM: 300948; MGI: 2147987; HomoloGene: 3564; GeneCards: PCYT1B; OMA:PCYT1B - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for PCYT1B
Genomic location for PCYT1B
BandXp22.11Start24,558,087 bp[1]
End24,672,677 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for PCYT1B
Genomic location for PCYT1B
BandX|X C3Start92,698,469 bp[2]
End92,793,557 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • ganglionic eminence

  • prefrontal cortex

  • C1 segment

  • amygdala

  • nucleus accumbens

  • left testis

  • cingulate gyrus

  • anterior cingulate cortex

  • right testis
Top expressed in
  • zygote

  • secondary oocyte

  • otolith organ

  • utricle

  • ganglionic eminence

  • dentate gyrus of hippocampal formation granule cell

  • piriform cortex

  • otic vesicle

  • respiratory epithelium

  • olfactory epithelium
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • nucleotidyltransferase activity
  • catalytic activity
  • transferase activity
  • choline-phosphate cytidylyltransferase activity
  • phosphatidylcholine binding
Cellular component
  • endoplasmic reticulum membrane
  • cytoplasm
  • endoplasmic reticulum
Biological process
  • phospholipid biosynthetic process
  • phosphatidylcholine biosynthetic process
  • biosynthesis
  • spermatogenesis
  • ovarian follicle development
  • lipid metabolism
  • CDP-choline pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9468

236899

Ensembl

ENSG00000102230

ENSMUSG00000035246

UniProt

Q9Y5K3

Q811Q9

RefSeq (mRNA)

NM_001163264
NM_001163265
NM_004845

NM_177546
NM_211138

RefSeq (protein)

NP_001156736
NP_001156737
NP_004836

NP_808214
NP_997593

Location (UCSC)Chr X: 24.56 – 24.67 MbChr X: 92.7 – 92.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Choline-phosphate cytidylyltransferase B is an enzyme that in humans is encoded by the PCYT1B gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000102230 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035246 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lykidis A, Murti KG, Jackowski S (Jul 1998). "Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase". J Biol Chem. 273 (22): 14022–9. doi:10.1074/jbc.273.22.14022. PMID 9593753.
  6. ^ "Entrez Gene: PCYT1B phosphate cytidylyltransferase 1, choline, beta".

Further reading

  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Llorca O, Martín-Benito J, Gómez-Puertas P, et al. (2002). "Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin". J. Struct. Biol. 135 (2): 205–18. doi:10.1006/jsbi.2001.4359. PMID 11580270.
  • McCormack EA, Llorca O, Carrascosa JL, et al. (2002). "Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT". J. Struct. Biol. 135 (2): 198–204. doi:10.1006/jsbi.2001.4385. PMID 11580269.
  • Lykidis A, Baburina I, Jackowski S (1999). "Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant". J. Biol. Chem. 274 (38): 26992–7001. doi:10.1074/jbc.274.38.26992. PMID 10480912.
  • Gubin AN, Njoroge JM, Bouffard GG, Miller JL (1999). "Gene expression in proliferating human erythroid cells". Genomics. 59 (2): 168–77. doi:10.1006/geno.1999.5855. PMID 10409428.
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